Oligomeric Structure and Tissue Distribution of Ficolins from Mouse, Pig and Human

Ohashi, Tomoo; Erickson, Harold P.

doi:10.1006/abbi.1998.0957

Cited by 89 publications

(65 citation statements)

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“…Ficolins ␣, L, H, and A have been purified from plasma, and their expression has been confirmed in the liver (2,3,8). SP-A and SP-D are expressed in the lung, as are ficolins ␣, M, and H (8,(12)(13)(14).…”

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confidence: 93%

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The Disulfide Bonding Pattern in Ficolin Multimers

Ohashi

Erickson

2004

Journal of Biological Chemistry

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Ficolin is a plasma lectin, consisting of a short Nterminal multimerization domain, a middle collagen domain, and a C-terminal fibrinogen-like domain. The collagen domains assemble the subunits into trimers, and the N-terminal domain assembles four trimers into 12-mers. Two cysteine residues in the N-terminal domain are thought to mediate multimerization by disulfide bonding. We have generated three mutants of ficolin ␣ in which the N-terminal cysteines were substituted by serines (Cys 4 , Cys 24 , and Cys 4 /Cys 24 ). The N-terminal cysteine mutants were produced in a mammalian cell expression system, purified by affinity chromatography, and analyzed under nondenaturing conditions to resolve the multimer structure of the native protein and under denaturing conditions to resolve the disulfidelinked structure. Glycerol gradient sedimentation and electron microscopy in nondenaturing conditions showed that plasma and recombinant wild-type protein formed 12-mers.

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confidence: 93%

“…In the past decade, many ficolin family proteins have been discovered in several species including pig (ficolins ␣ and ␤) (1), human (ficolins H, L, and M) (2-6), mouse (ficolins A and B) (7,8), and frog (ficolins 1-4) (9). Ficolin-like proteins have been reported in invertebrates such as horseshoe crab and the solitary ascidian (10,11).…”

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confidence: 99%

The Disulfide Bonding Pattern in Ficolin Multimers

Ohashi

Erickson

2004

Journal of Biological Chemistry

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“…Three types of ficolins have recently been identified in human, L-ficolin/P35 (FCN2 or ficolin 2) (12), M-ficolin (FCN1 or ficolin 1) (13,14), and H-ficolin/Hakata antigen (FCN3 or ficolin 3) (15)(16)(17), and two types of ficolins, ficolins A and B, have been identified in mice (18,19). The fibrinogen-like domain of L-ficolin, forming a globular structure like the CRD of MBL, is the pattern of carbohydrate structures.…”

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confidence: 99%

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Liu

Ali

et al. 2009

Cell Mol Immunol

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L-ficolin, one of lectin families, is a recently identified complement factor that initiates lectin pathway of complement. Little is known about its role in viral hepatitis. In the present study, we found that L-ficolin in serum from 103 patients with hepatitis C virus (HCV), were significantly higher than that in 150 healthy controls. We further found that L-ficolin expressions were significantly increased in vitro study by HCV JFH-1 infected human hepatocyte cell line Huh7.5.

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“…3 The C-terminal end of the molecule, the globular fibrinogen-like domain, is responsible for ligand recognition. [3][4][5] Although the ficolins share a common preference for acetylated compounds, each ficolin displays distinct ligand specificities. Ficolin-2 binds to a wide range of pathogens, such as bacteria, fungi and viruses, whereas only a few bacterial ligands have been identified for ficolin-3.…”

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Variation in FCN1 affects biosynthesis of ficolin-1 and is associated with outcome of systemic inflammation

et al. 2012

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Ficolin-1 is a recognition molecule of the lectin complement pathway. The ficolin-1 gene FCN1 is polymorphic, but the functional and clinical consequences are unknown.The concentration of ficolin-1 in plasma and FCN1 polymorphisms in positions À 1981 (rs2989727), À 791 (rs28909068), À 542 (rs10120023), À 271 (rs28909976), À 144 (rs10117466) and þ 7918 (rs1071583) were determined in 100 healthy individuals. FCN1 expression by isolated monocytes and granulocytes and ficolin-1 levels in monocyte culture supernatants were assessed in 21 FCN1-genotyped individuals. FCN1 polymorphisms were determined in a cohort of 251 patients with systemic inflammation. High ficolin-1 plasma levels were significantly associated with the minor alleles in position À 542 and À 144. These alleles were also significantly associated with high FCN1 mRNA expression. The level of ficolin-1 in culture supernatants was significantly higher in individuals homozygous for the minor alleles at positions À 542 and À 144. Homozygosity for these alleles was significantly associated with fatal outcome in patients with systemic inflammation. None of the other investigated polymorphisms were associated with FCN1 and ficolin-1 expression, concentration or disease outcome. Functional polymorphic sites in the promoter region of FCN1 regulate both the expression and synthesis of ficolin-1 and are associated with outcome in severe inflammation.

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Oligomeric Structure and Tissue Distribution of Ficolins from Mouse, Pig and Human

Cited by 89 publications

References 28 publications

The Disulfide Bonding Pattern in Ficolin Multimers

The Disulfide Bonding Pattern in Ficolin Multimers

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Variation in FCN1 affects biosynthesis of ficolin-1 and is associated with outcome of systemic inflammation

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